Q9PZT0
Gene name |
vp |
Protein name |
Minor capsid protein VP1 |
Names |
Coat protein VP1 |
Species |
Human parvovirus B19 (strain HV) (HPV B19) |
KEGG Pathway |
vg:11293627 |
EC number |
3.1.1.4: Carboxylic ester hydrolases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9PZT0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1S58 | X-ray | 350 A | A | 1-554 | PDB |
No variants for Q9PZT0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9PZT0 | |||||
No associated diseases with Q9PZT0
Functions
| Description | ||
|---|---|---|
| EC Number | 3.1.1.4 | Carboxylic ester hydrolases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| host cell cytoplasm | The cytoplasm of a host cell. |
| host cell nucleus | A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction. |
| T=1 icosahedral viral capsid | The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=1 symmetry. The T=1 capsid is composed of 12 pentameric capsomeres. |
| viral capsid | The protein coat that surrounds the infective nucleic acid in some virus particles. It comprises numerous regularly arranged subunits, or capsomeres. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| phospholipase A2 activity | Catalysis of the reaction: a 1,2-diacyl-sn-glycero-3-phospholipid + H2O = 1-acyl-sn-glycero-3-phospholipid + a fatty acid. This reaction removes the fatty acid attached to the sn2-position. Substrates include phosphatidylcholine, phosphatidylethanolamine, choline plasmalogen and phosphatides. |
| structural molecule activity | The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| clathrin-dependent endocytosis of virus by host cell | Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus. |
| lipid catabolic process | The chemical reactions and pathways resulting in the breakdown of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. |
| microtubule-dependent intracellular transport of viral material towards nucleus | The directed movement of a virus, or part of a virus, towards the host cell nucleus using host microtubules. |
| permeabilization of host organelle membrane involved in viral entry into host cell | Induction of organellar membrane permeabilization triggered by an interaction between the host membrane and a membrane-penetration protein associated with a viral capsid. Results in release of the virus contents from an organelle into the host cell cytoplasm. |
| receptor-mediated virion attachment to host cell | The process by which a virion attaches to a host cell by binding to a receptor on the host cell surface. |
| viral entry via permeabilization of inner membrane | The entry of a non-enveloped virus into the cytoplasm of a host prokaryotic cell, following fusion with the outer membrane, via permeabilization of the plasma (inner) membrane. In the case of some double stranded RNA viruses of prokaryotes this occurs via interaction of a membrane-interacting component of the capsid, leading to depolarization an permeabilization of the plasma membrane. |
| viral penetration into host nucleus | The crossing by the virus of the host nuclear membrane, either as naked viral genome or for small viruses as an intact capsid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSKESGKWWE | SDDKFAKAVY | QQFVEFYEKV | TGTDLELIQI | LKDHYNISLD | NPLENPSSLF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLVARIKNNL | KNSPDLYSHH | FQSHGQLSDH | PHALSSSSSH | AEPRGENAVL | SSEDLHKPGQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VSVQLPGTNY | VGPGNELQAG | PPQSAVDSAA | RIHDFRYSQL | AKLGINPYTH | WTVADEELLK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NIKNETGFQA | QVVKDYFTLK | GAAAPVAHFQ | GSLPEVPAYN | ASEKYPSMTS | VNSAEASTGA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GGGGSNPVKS | MWSEGATFSA | NSVTCTFSRQ | FLIPYDPEHH | YKVFSPAASS | CHNASGKEAK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VCTISPIMGY | STPWRYLDFN | ALNLFFSPLE | FQHLIENYGS | IAPDALTVTI | SEIAVKDVTD |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KTGGGVQVTD | STTGRLSMLV | DHEYKYPYVL | GQGQDTLAPE | LPIWVYFPPQ | YAYLTVGDVN |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TQGISGDSKK | LASEESAFYV | LEHSSFQLLG | TGGTATMSYK | FPPVPPENLE | GCSQHFYEMY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NPLYGSRLGV | PDTLGGDPKF | RSLTHEDHAI | QPQNFMPGPL | VNSVSTKEGD | SSNTGAGKAL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TGLSTGTSQN | TRISLRPGPV | SQPYHHWDTD | KYVPGINAIS | HGQTTYGNAE | DKEYQQGVGR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FPNEKEQLKQ | LQGLNMHTYF | PNKGTQQYTD | QIERPLMVGS | VWNRRALHYE | SQLWSKIPNL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DDSFKTQFAA | LGGWGLHQPP | PQIFLKILPQ | SGPIGGIKSM | GITTLVQYAV | GIMTVTMTFK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| LGPRKATGRW | NPQPGVYPPH | AAGHLPYVLY | DPTATDAKQH | HRHGYEKPEE | LWTAKSRVHP |
| L |